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Table 1 Data collection and refinement statistics.

From: Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx

Data collection

   

   Beamline

DESY X12

   Temperature (K)

100

   Dataset type

Peak

Inflection point

High-energy remote

   Wavelength (Å)

1.10371

1.10420

1.10009

   Data range (°)

180

   Oscillation range (°)

0.5

   Space group

P31

   Unit cell parameters (Å)

a = b = 53.0, c = 143.5

   Resolution (Å)

20 to 2.8 (2.95 to 2.8)

   Unique reflections

19,800 (3,352)

19,790 (3,392)

19,765 (3,365)

   Redundancy

2.84 (2.84)

2.83 (2.82)

2.84 (2.84)

   Completeness (%)

90.0 (94.5)

89.9 (96.9)

89.7 (95.9)

   Mean I/σI

16.5 (3.45)

15.52 (2.92)

18.19 (3.84)

   Rmergea

0.05 (0.30)

0.06 (0.40)

0.05 (0.28)

   Mosaicity (°)

0.271

   Estimated Wilson B2)

54.1

Refinement

   

   R work b

0.2271

   R free c

0.2508

Molecules in the asymmetric unit

(DC-LAMP/GlcNAc/Ir)

2/2/4

   No. of atoms

   

Protein

2,438

Hetero atoms

32

Water

10

Total

2,480

   Atomic displacement factor B2)

61.3

   Real space correlation coefficientd

0.882

   r.m.s.d. from ideal

   

Bond lengths (Å)

0.0056

Bond angles (°)

1.023

   Ramachandran plot

   

Favored (%)

90.9

Allowed (%)

6.8

Disallowed (%)

2.3

  1. Values in parentheses account for the highest resolution shell.
  2. a R m e r g e = h k l i I h k l , i - I h k l ¯ h k l i I h k l , i
  3. b R w o r k = h k l F o b s - F c a l c h k l F o b s
  4. c R free is calculated as R work but using F obs derived from 5% randomly selected reflections exclude from refinement.
  5. d R S C C = x y z ρ o - ρ o ¯ x y z ρ c - ρ c ¯ / x y z ρ o - ρ o ¯ 2 x y z ρ c - ρ c ¯ 2 1 / 2